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HAMAP rule MF_03019

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General rule information [?]

Accession MF_03019
Dates 12-FEB-2009 (Created)
1-JUN-2023 (Last updated, Version 15)
Name 3_HAO_euk
Scope(s) Eukaryota
Template(s) Q0VCA8 (3HAO_BOVIN); Q78JT3 (3HAO_MOUSE); Q54S02 (3HAO_DICDI); P46952 (3HAO_HUMAN); P47096 (3HAO_YEAST); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_00825 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier 3HAO
case <OC:Fungi>
Protein name RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase;
                 EC=1.13.11.6;
AltName: Full=3-hydroxyanthranilate oxygenase;
                 Short=3-HAO;
AltName: Full=3-hydroxyanthranilic acid dioxygenase;
                 Short=HAD;
AltName: Full=Biosynthesis of nicotinic acid protein 1;
else
Protein name RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase;
                 EC=1.13.11.6;
AltName: Full=3-hydroxyanthranilate oxygenase;
                 Short=3-HAO;
AltName: Full=3-hydroxyanthranilic acid dioxygenase;
                 Short=HAD;
end case
case <OC:Vertebrata>
Gene name Name=HAAO;
else case <OC:Fungi>
Gene name Name=BNA1;
end case

Comments [?]

FUNCTIONCatalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
CATALYTIC ACTIVITY Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379, ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6;
case <FTGroup:1> or <FTGroup:2>
COFACTOR Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
end case
PATHWAYCofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
case <OC:Vertebrata>
SUBUNITMonomer.
end case
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the 3-HAO family.

Keywords [?]

Dioxygenase
Oxidoreductase
Pyridine nucleotide biosynthesis
case <OC:Eukaryota>
Cytoplasm
end case
case <FTGroup:1> or <FTGroup:2>
Iron
end case
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3>
Metal-binding
end case

Gene Ontology [?]

GO:0000334; Molecular function:3-hydroxyanthranilate 3,4-dioxygenase activity
GO:0008198; Molecular function:ferrous iron binding
GO:0006569; Biological process:tryptophan catabolic process
GO:0019805; Biological process:quinolinate biosynthetic process
GO:0034354; Biological process:'de novo' NAD biosynthetic process from tryptophan
GO:0043420; Biological process:anthranilate metabolic process
case <OCellular component:Eukaryota>
GO:0005737; Cellular component:cytoplasm
end case

Cross-references [?]

Pfam PF06052; 3-HAO; 1;
NCBIfam TIGR03037; Anthran_nbaC; 1;

Features [?]

From: 3HAO_BOVIN (Q0VCA8)
Key From To Description Tag Condition FTGroup
case <OC:Metazoa>
REGION Nter 160 /note="Domain A (catalytic)"
REGION 161 177 /note="Linker"
REGION 178 Cter /note="Domain B"
BINDING 47 47 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 1
BINDING 53 53 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 E 1
BINDING 91 91 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 1
BINDING 43 43 /ligand="O2"
/ligand_id="ChEBI:CHEBI:15379"		 R
BINDING 53 53 /ligand="substrate" E
BINDING 95 95 /ligand="substrate" R
BINDING 105 105 /ligand="substrate" E
end case
From: 3HAO_YEAST (P47096)
Key From To Description Tag Condition FTGroup
case <OC:Fungi>
BINDING 49 49 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 2
BINDING 55 55 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 E 2
BINDING 97 97 /ligand="Fe cation"
/ligand_id="ChEBI:CHEBI:24875"
/ligand_note="catalytic"		 H 2
BINDING 126 126 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 C 3
BINDING 129 129 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 C 3
BINDING 163 163 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 C 3
BINDING 166 166 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 C 3
BINDING 45 45 /ligand="O2"
/ligand_id="ChEBI:CHEBI:15379"		 R
BINDING 55 55 /ligand="substrate" E
BINDING 101 101 /ligand="substrate" R
BINDING 111 111 /ligand="substrate" E
end case

Additional information [?]

Size range 160-288 amino acids
Related rules None
Fusion Nter: None Cter: None



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